Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
about
Dynamic mechanism of proton transfer in mannitol 2-dehydrogenase from Pseudomonas fluorescens: mobile GLU292 controls proton relay through a water channel that connects the active site with bulk solvent.Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.Structural and mechanistic basis of differentiated inhibitors of the acute pancreatitis target kynurenine-3-monooxygenaseUnderstanding the broad substrate repertoire of nitroreductase based on its kinetic mechanism.Tyr217 and His213 are important for substrate binding and hydroxylation of 3-hydroxybenzoate 6-hydroxylase fromRhodococcus jostiiRHA1
P2860
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
description
2005 nî lūn-bûn
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2005年の論文
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2005年学术文章
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name
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@en
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@nl
type
label
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@en
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@nl
prefLabel
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@en
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@nl
P356
P1433
P1476
Kinetics of proton-linked flavin conformational changes in p-hydroxybenzoate hydroxylase.
@en
P2093
Kendra King Frederick
P304
13304-13314
P356
10.1021/BI051119T
P407
P50
P577
2005-10-01T00:00:00Z